Tag | Content |
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CPLM ID | CPLM-003345 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Bifunctional protein GlmU |
Protein Synonyms/Alias | UDP-N-acetylglucosamine pyrophosphorylase; N-acetylglucosamine-1-phosphate uridyltransferase; Glucosamine-1-phosphate N-acetyltransferase |
Gene Name | glmU |
Gene Synonyms/Alias | yieA; b3730; JW3708 |
Created Date | July 27, 2013 |
Organism | Escherichia coli (strain K12) |
NCBI Taxa ID | 83333 |
Lysine Modification | Position | Peptide | Type | References |
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25 | RMYSDLPKVLHTLAG | acetylation | [1] | 63 | GHGGDLLKQALKDDN | acetylation | [1] | 132 | GIGLLTVKLDDPTGY | acetylation | [1] | 156 | VTGIVEHKDATDEQR | acetylation | [1] | 246 | YQSEQAEKLLLAGVM | acetylation | [1] | 351 | VGNFVEMKKARLGKG | acetylation | [1, 2] | 360 | ARLGKGSKAGHLTYL | acetylation | [1] | 392 | CNYDGANKFKTIIGD | acetylation | [1] |
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Reference | [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli. Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C. Mol Cell. 2013 Jul 25;51(2):265-72. [ PMID: 23830618] [2] Comprehensive profiling of protein lysine acetylation in Escherichia coli. Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z. J Proteome Res. 2013 Feb 1;12(2):844-51. [ PMID: 23294111] |
Functional Description | Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP- GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5- monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. |
Sequence Annotation | REGION 1 229 Pyrophosphorylase. REGION 11 14 UDP-GlcNAc binding. REGION 81 82 UDP-GlcNAc binding. REGION 103 105 UDP-GlcNAc binding. REGION 230 250 Linker. REGION 251 456 N-acetyltransferase. REGION 386 387 Acetyl-CoA binding. ACT_SITE 363 363 Proton acceptor (By similarity). METAL 105 105 Magnesium. METAL 227 227 Magnesium. BINDING 25 25 UDP-GlcNAc (By similarity). BINDING 76 76 UDP-GlcNAc. BINDING 140 140 UDP-GlcNAc; via amide nitrogen. BINDING 154 154 UDP-GlcNAc. BINDING 169 169 UDP-GlcNAc. BINDING 227 227 UDP-GlcNAc (By similarity). BINDING 333 333 UDP-GlcNAc. BINDING 351 351 UDP-GlcNAc. BINDING 366 366 UDP-GlcNAc. BINDING 377 377 UDP-GlcNAc. BINDING 380 380 Acetyl-CoA; via amide nitrogen. BINDING 405 405 Acetyl-CoA. BINDING 423 423 Acetyl-CoA; via amide nitrogen. BINDING 440 440 Acetyl-CoA. |
Keyword | 3D-structure; Acyltransferase; Cell shape; Cell wall biogenesis/degradation; Cobalt; Complete proteome; Cytoplasm; Magnesium; Metal-binding; Multifunctional enzyme; Nucleotidyltransferase; Peptidoglycan synthesis; Reference proteome; Repeat; Transferase. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 456 AA |
Protein Sequence | MLNNAMSVVI LAAGKGTRMY SDLPKVLHTL AGKAMVQHVI DAANELGAAH VHLVYGHGGD 60 LLKQALKDDN LNWVLQAEQL GTGHAMQQAA PFFADDEDIL MLYGDVPLIS VETLQRLRDA 120 KPQGGIGLLT VKLDDPTGYG RITRENGKVT GIVEHKDATD EQRQIQEINT GILIANGADM 180 KRWLAKLTNN NAQGEYYITD IIALAYQEGR EIVAVHPQRL SEVEGVNNRL QLSRLERVYQ 240 SEQAEKLLLA GVMLRDPARF DLRGTLTHGR DVEIDTNVII EGNVTLGHRV KIGTGCVIKN 300 SVIGDDCEIS PYTVVEDANL AAACTIGPFA RLRPGAELLE GAHVGNFVEM KKARLGKGSK 360 AGHLTYLGDA EIGDNVNIGA GTITCNYDGA NKFKTIIGDD VFVGSDTQLV APVTVGKGAT 420 IAAGTTVTRN VGENALAISR VPQTQKEGWR RPVKKK 456 |
Gene Ontology | GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IDA:EcoCyc. GO:0042802; F:identical protein binding; IDA:EcoCyc. GO:0000287; F:magnesium ion binding; IDA:EcoCyc. GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IDA:EcoCyc. GO:0000902; P:cell morphogenesis; IEA:HAMAP. GO:0009245; P:lipid A biosynthetic process; IEA:UniProtKB-UniPathway. GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro. GO:0009252; P:peptidoglycan biosynthetic process; IEA:HAMAP. GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW. GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IMP:EcoCyc. |
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